1zbl: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1zbl.gif|left|200px]]
{{Seed}}
[[Image:1zbl.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zbl|  PDB=1zbl  |  SCENE=  }}  
{{STRUCTURE_1zbl|  PDB=1zbl  |  SCENE=  }}  


'''Bacillus halodurans RNase H catalytic domain mutant D192N in complex with 12-mer RNA/DNA hybrid'''
===Bacillus halodurans RNase H catalytic domain mutant D192N in complex with 12-mer RNA/DNA hybrid===




==Overview==
<!--
RNase H belongs to a nucleotidyl-transferase superfamily, which includes transposase, retroviral integrase, Holliday junction resolvase, and RISC nuclease Argonaute. We report the crystal structures of RNase H complexed with an RNA/DNA hybrid and a mechanism for substrate recognition and two-metal-ion-dependent catalysis. RNase H specifically recognizes the A form RNA strand and the B form DNA strand. Structure comparisons lead us to predict the catalytic residues of Argonaute and conclude that two-metal-ion catalysis is a general feature of the superfamily. In nucleases, the two metal ions are asymmetrically coordinated and have distinct roles in activating the nucleophile and stabilizing the transition state. In transposases, they are symmetrically coordinated and exchange roles to alternately activate a water and a 3'-OH for successive strand cleavage and transfer by a ping-pong mechanism.
The line below this paragraph, {{ABSTRACT_PUBMED_15989951}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15989951 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15989951}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Rna/dna hybrid]]
[[Category: Rna/dna hybrid]]
[[Category: Rnase h]]
[[Category: Rnase h]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:25:34 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 10 12:35:02 2008''